OAZ_AEDAE
ID OAZ_AEDAE Reviewed; 240 AA.
AC Q95P51; Q17BZ2; Q8T4Q6; Q95P52;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Ornithine decarboxylase antizyme;
DE Short=ODC-Az;
GN Name=Oda; ORFNames=AAEL004783;
OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7159;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Moyo-R, and Red eye; TISSUE=Midgut;
RX PubMed=14513362; DOI=10.1007/s00438-003-0882-7;
RA Morlais I., Mori A., Schneider J.R., Severson D.W.;
RT "A targeted approach to the identification of candidate genes determining
RT susceptibility to Plasmodium gallinaceum in Aedes aegypti.";
RL Mol. Genet. Genomics 269:753-764(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Moyo-R;
RA Morlais I., Severson D.W.;
RT "Single nucleotide polymorphism and codon usage bias in Aedes aegypti.";
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LVPib12;
RX PubMed=17510324; DOI=10.1126/science.1138878;
RA Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL Science 316:1718-1723(2007).
CC -!- FUNCTION: Ornithine decarboxylase (ODC) antizyme protein that
CC negatively regulates ODC activity and intracellular polyamine
CC biosynthesis and uptake in response to increased intracellular
CC polyamine levels. Binds to ODC monomers, inhibiting the assembly of the
CC functional ODC homodimer, and targets the monomers for ubiquitin-
CC independent proteolytic destruction by the 26S proteasome.
CC {ECO:0000250|UniProtKB:P54368}.
CC -!- SUBUNIT: Interacts with ODC1 and thereby sterically blocks ODC
CC homodimerization. {ECO:0000250|UniProtKB:P54368}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=1;
CC Comment=A ribosomal frameshift occurs between the codons for Ser-61
CC and Asp-62. An autoregulatory mechanism enables modulation of
CC frameshifting according to the cellular concentration of polyamines.;
CC Name=1;
CC IsoId=Q95P51-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Preferentially expressed in adult female midguts.
CC {ECO:0000269|PubMed:14513362}.
CC -!- SIMILARITY: Belongs to the ODC antizyme family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAT43827.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF396870; AAK85383.1; -; mRNA.
DR EMBL; AF396871; AAK85384.1; -; mRNA.
DR EMBL; AY064120; AAL85621.2; -; mRNA.
DR EMBL; AY133346; AAN11326.1; -; mRNA.
DR EMBL; CH477314; EAT43827.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001649725.1; XM_001649675.2. [Q95P51-1]
DR AlphaFoldDB; Q95P51; -.
DR SMR; Q95P51; -.
DR STRING; 7159.AAEL004783-PA; -.
DR GeneID; 5565400; -.
DR KEGG; aag:5565400; -.
DR VEuPathDB; VectorBase:AAEL004783; -.
DR eggNOG; KOG4387; Eukaryota.
DR HOGENOM; CLU_1058742_0_0_1; -.
DR InParanoid; Q95P51; -.
DR OrthoDB; 1403675at2759; -.
DR Proteomes; UP000008820; Chromosome 2.
DR GO; GO:0008073; F:ornithine decarboxylase inhibitor activity; IEA:InterPro.
DR Gene3D; 3.40.630.60; -; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR002993; ODC_AZ.
DR InterPro; IPR038581; ODC_AZ_sf.
DR PANTHER; PTHR10279; PTHR10279; 1.
DR Pfam; PF02100; ODC_AZ; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS01337; ODC_AZ; 1.
PE 2: Evidence at transcript level;
KW Reference proteome; Ribosomal frameshifting.
FT CHAIN 1..240
FT /note="Ornithine decarboxylase antizyme"
FT /id="PRO_0000311434"
FT REGION 18..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 69..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 15
FT /note="L -> Q (in Ref. 2; AAL85621)"
FT /evidence="ECO:0000305"
FT CONFLICT 18
FT /note="R -> W (in Ref. 2; AAL85621)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="L -> P (in Ref. 1; AAK85383)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 240 AA; 27170 MW; 27D758FE4E92B5D6 CRC64;
MMKFVASEIS SIMELQMRSE PISSSNRATK RTISSSSSSS SSSAGFDSYC VSLAVGPLWW
SDVPQSRTDH DRASPLKEYN RKTSIDSTTT ASSEFTDYDD TESTVEFMNQ HEAAVIQEVL
NQPTPTQISL KLFVTPQKYS VWETVFNPLD NILYVNLPST MTHEASKHSF ISLLEFAEEK
LECDAVVLCI RKDRLDRPNL VRTFSFVGFQ PVSPKSPLAP PHIEEQQKND YLFMIYNIEE
